Extended Data Fig. 6: RPA constrains the dynamics of the RAD52-mediated DNA strand exchange at the fork but does not reduce its efficiency.
From: The RAD52 double-ring remodels replication forks restricting fork reversal
a. Cartoon depiction of the experimental design. A model replication fork with a leading strand gap was assembled from oligonucleotides #2, #7, #8 and #9 (homologous fork), #2, #7, #9 and #10 (four-way junction), or #2, #8, #9 and #11 (heterologous fork) listed in Supplemental Table 1. The Cy3 (FRET donor) and Cy5 (FRET acceptor) dyes are placed at the lagging and leading arms of the fork (FRET 0.26). b-d. Single-molecule FRET distributions for the forks containing two fully homologous arms (homologous fork) (b), fully exchanged fork (4-way junction) (c), and heterologous fork (the ssDNA gap region consists of 30 Ts) (d). Note that the peak around 0 FRET corresponds to the molecules with bleached Cy5 dye which accumulate over time. e. A representative smFRET trajectory for the RAD52-mediated strand exchange reaction in the presence of RPA.
